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Literature DB >> 11357630

Modeling the native state ensemble.

V J Hilser¹.

Abstract

Mesh：

Substances：
Amino Acids

Year: 2001 PMID： 11357630 DOI： 10.1385/1-59259-193-0:093

Source DB: PubMed Journal: Methods Mol Biol ISSN： 1064-3745

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12 in total

1. Local conformational fluctuations can modulate the coupling between proton binding and global structural transitions in proteins.

Authors: Steven T Whitten; Bertrand García-Moreno E; Vincent J Hilser
Journal: Proc Natl Acad Sci U S A Date: 2005-03-14 Impact factor: 11.205

2. Functional residues serve a dominant role in mediating the cooperativity of the protein ensemble.

Authors: Tong Liu; Steven T Whitten; Vincent J Hilser
Journal: Proc Natl Acad Sci U S A Date: 2007-03-05 Impact factor: 11.205

3. Quantitative assessment of protein structural models by comparison of H/D exchange MS data with exchange behavior accurately predicted by DXCOREX.

Authors: Tong Liu; Dennis Pantazatos; Sheng Li; Yoshitomo Hamuro; Vincent J Hilser; Virgil L Woods
Journal: J Am Soc Mass Spectrom Date: 2011-10-20 Impact factor: 3.109

4. Global distribution of conformational states derived from redundant models in the PDB points to non-uniqueness of the protein structure.

Authors: Prasad V Burra; Ying Zhang; Adam Godzik; Boguslaw Stec
Journal: Proc Natl Acad Sci U S A Date: 2009-06-24 Impact factor: 11.205

Modeling the native state ensemble.

1. Local conformational fluctuations can modulate the coupling between proton binding and global structural transitions in proteins.

2. Functional residues serve a dominant role in mediating the cooperativity of the protein ensemble.

3. Quantitative assessment of protein structural models by comparison of H/D exchange MS data with exchange behavior accurately predicted by DXCOREX.

4. Global distribution of conformational states derived from redundant models in the PDB points to non-uniqueness of the protein structure.

Review 5. What Mutagenesis Can and Cannot Reveal About Allostery.

Review 6. The role of protein conformational fluctuations in allostery, function, and evolution.

7. H/D Exchange Characterization of Silent Coupling: Entropy-Enthalpy Compensation in Allostery.

8. Protein hydrogen exchange: testing current models.

9. Protein dynamics viewed by hydrogen exchange.

10. Energetic profiling of protein folds.